RASF1_CAEEL
ID RASF1_CAEEL Reviewed; 615 AA.
AC Q22744; Q58AA9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ras association domain-containing protein 1 homolog {ECO:0000305|PubMed:23103556};
GN Name=rsf-1 {ECO:0000303|PubMed:23103556, ECO:0000312|WormBase:T24F1.3a};
GN Synonyms=rasf-1 {ECO:0000303|PubMed:23294242,
GN ECO:0000312|WormBase:T24F1.3a};
GN ORFNames=T24F1.3 {ECO:0000312|WormBase:T24F1.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH RAB-39, TISSUE SPECIFICITY (ISOFORM A), AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23294242; DOI=10.1111/gtc.12028;
RA Takenaka M., Inoue H., Takeshima A., Kakura T., Hori T.;
RT "C. elegans Rassf homolog, rasf-1, is functionally associated with rab-39
RT Rab GTPase in oxidative stress response.";
RL Genes Cells 18:203-210(2013).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CST-1, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=23103556; DOI=10.1016/j.yexcr.2012.10.008;
RA Iwasa H., Kuroyanagi H., Maimaiti S., Ikeda M., Nakagawa K., Hata Y.;
RT "Characterization of RSF-1, the Caenorhabditis elegans homolog of the Ras-
RT association domain family protein 1.";
RL Exp. Cell Res. 319:1-11(2013).
CC -!- FUNCTION: Involved in embryonic morphogenesis (PubMed:23103556). Plays
CC a role in the organization of apical filamentous actin in epithelial
CC cells of the developing embryo (PubMed:23103556). May play a role in
CC let-60-mediated vulval development (PubMed:23103556). May induce
CC nuclear condensation (PubMed:23103556). Positively regulates the
CC oxidative stress response, and this may be in association with the
CC small GTPase rab-39 (PubMed:23294242). Not required for muscle
CC integrity (PubMed:23103556). {ECO:0000269|PubMed:23103556,
CC ECO:0000269|PubMed:23294242}.
CC -!- SUBUNIT: Interacts with rab-39 (GTP-bound form) (PubMed:23294242).
CC Interacts (via SARAH domain) with cst-1; the interaction is required
CC for the phosphorylation of cst-1 (PubMed:23103556).
CC {ECO:0000269|PubMed:23103556, ECO:0000269|PubMed:23294242}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9NS23}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:T24F1.3a}; Synonyms=rasf-1a
CC {ECO:0000303|PubMed:23294242};
CC IsoId=Q22744-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:T24F1.3b}; Synonyms=rasf-1b
CC {ECO:0000303|PubMed:23294242};
CC IsoId=Q22744-2; Sequence=VSP_061059;
CC -!- TISSUE SPECIFICITY: Expressed in the pharynx, epithelial cells,
CC ciliated neurons in the head, body wall muscles, hypodermis, vulva,
CC gonadal sheath cells, tail hypodermis and in coelomocytes.
CC {ECO:0000269|PubMed:23103556}.
CC -!- TISSUE SPECIFICITY: [Isoform a]: Expressed in the pharynx, neurons and
CC vulva. {ECO:0000269|PubMed:23294242}.
CC -!- DEVELOPMENTAL STAGE: In embryos, expressed in epidermal cells during
CC the dorsal intercalation and ventral enclosure.
CC {ECO:0000269|PubMed:23103556}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC survival in response to oxidative stress induced by sodium arsenite.
CC {ECO:0000269|PubMed:23294242}.
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DR EMBL; BX284602; CAA90137.1; -; Genomic_DNA.
DR EMBL; BX284602; CAI70412.1; -; Genomic_DNA.
DR PIR; T25245; T25245.
DR RefSeq; NP_001022361.1; NM_001027190.4. [Q22744-1]
DR RefSeq; NP_001022362.1; NM_001027191.3.
DR AlphaFoldDB; Q22744; -.
DR SMR; Q22744; -.
DR STRING; 6239.T24F1.3a; -.
DR EPD; Q22744; -.
DR PaxDb; Q22744; -.
DR PeptideAtlas; Q22744; -.
DR EnsemblMetazoa; T24F1.3a.1; T24F1.3a.1; WBGene00011995. [Q22744-1]
DR EnsemblMetazoa; T24F1.3b.1; T24F1.3b.1; WBGene00011995. [Q22744-2]
DR EnsemblMetazoa; T24F1.3b.2; T24F1.3b.2; WBGene00011995. [Q22744-2]
DR GeneID; 174728; -.
DR KEGG; cel:CELE_T24F1.3; -.
DR UCSC; T24F1.3a; c. elegans.
DR CTD; 174728; -.
DR WormBase; T24F1.3a; CE02363; WBGene00011995; rsf-1. [Q22744-1]
DR WormBase; T24F1.3b; CE38227; WBGene00011995; rsf-1. [Q22744-2]
DR eggNOG; KOG4239; Eukaryota.
DR GeneTree; ENSGT00940000169509; -.
DR HOGENOM; CLU_036241_0_0_1; -.
DR InParanoid; Q22744; -.
DR OMA; ALYECEQ; -.
DR OrthoDB; 1120975at2759; -.
DR PhylomeDB; Q22744; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00011995; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q22744; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IMP:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IMP:UniProtKB.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0040028; P:regulation of vulval development; IGI:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR033614; RASSF1-6.
DR InterPro; IPR011524; SARAH_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR22738; PTHR22738; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF16517; Nore1-SARAH; 1.
DR Pfam; PF00788; RA; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50951; SARAH; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Metal-binding; Microtubule;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..615
FT /note="Ras association domain-containing protein 1 homolog"
FT /id="PRO_0000452815"
FT DOMAIN 396..496
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 498..545
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT ZN_FING 164..214
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..61
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061059"
SQ SEQUENCE 615 AA; 69144 MW; BB72AC93DFF1EF76 CRC64;
MLRSVVNNND KAKESEQSVR VATDDPTYQS YAFQPSTSSS NISWFGGLRT KLSQLSLFPD
WMSQLGIKSD DEKMETSSTS SPQSEQSIGE YDESTLVFRP VQLDHFGGAG QEDDGEQVDI
WDFGATFLAD LDSNHVWNDT IERQHFGPLK DLITTGGGAN KINNHSFKTH SLLHPTWCDK
CGDFIWGILK EALKCEHCNY TCHARCRDLV TLDCRSPGSS LASSTEFDSI YPQLDGTLGT
IPKGLILPPA MSSSTGSDKE NGNGNSAGIS AENPIFSVKN SFTLPKSFSP VDSLRTKEPS
APPESRYATL RVVERYVKED TPFEWTDEYK EMDLERKIHS YNSLAKGMEI TLHEDGVNFG
GHIHVNMNLS RPISVVQGVI PPTVYDVVNT AKSTAKTTSL RTITSFFLPR NTAKVINIDS
KTTARKMIVT LLKKFRVADN PRKFALYECE QITDEATCTL NRKLTRISDD ACPLKVVLNW
QSPHCGRALV LQENDTGDIL WDAFEIPELE NFLRILGMEE KQYVFQTQQK YQQYRYHLDA
ELRQRGHSVP DAAAQPMVQT NPFLDEEFLR NQDEYGTSDS MLFSGTIKNA IMGEDPDYVN
LEYLKKQNMD QSTNL
